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Binding modes of thioflavin t molecules to prion peptide assemblies identified by using scanning tunneling microscopy

文献类型:期刊论文

作者Mao, Xiaobo1,2; Guo, Yuanyuan1,2; Wang, Chenxuan1,2; Zhang, Min1,2; Ma, Xiaojing1,2; Liu, Lei1,2; Niu, Lin1,2; Zeng, Qingdao1,2; Yang, Yanlian1,2; Wang, Chen1,2
刊名Acs chemical neuroscience
出版日期2011-06-01
卷号2期号:6页码:281-287
关键词Gnnqqny Thioflavin t Binding mode Amyloid Labeling molecule Scanning tunneling microscopy
ISSN号1948-7193
DOI10.1021/cn200006h
通讯作者Yang, yanlian(yangyl@nanoctr.cn)
英文摘要The widely used method to monitor the aggregation process of amyloid peptide is thioflavin t (tht) assay, while the detailed molecular mechanism is still not clear. in this work, we report here the direct identification of the binding modes of tht molecules with the prion peptide gnnqqny by using scanning tunneling microscopy (stm). the assembly structures of gnnqqny were first observed by stm on a graphite surface, and the introduction of tht molecules to the surface facilitated the stm observations of the adsorption conformations of tht with peptide strands. tht molecules are apt to adsorb on the peptide assembly with beta-sheet structure and oriented parallel with the peptide strands adopting four different binding modes. this effort could benefit the understanding of the mechanisms of the interactions between labeling species or inhibitory ligands and amyloid peptides, which is keenly needed for developing diagnostic and therapeutic approaches.
WOS关键词AMYLOID FIBRILS ; ALZHEIMERS-DISEASE ; CONGO RED ; DYNAMICS SIMULATIONS ; HIGH-AFFINITY ; PROTEIN ; MECHANISM ; DERIVATIVES ; INHIBITION ; TOXICITY
WOS研究方向Biochemistry & Molecular Biology ; Pharmacology & Pharmacy ; Neurosciences & Neurology
WOS类目Biochemistry & Molecular Biology ; Chemistry, Medicinal ; Neurosciences
语种英语
WOS记录号WOS:000291896800003
出版者AMER CHEMICAL SOC
URI标识http://www.irgrid.ac.cn/handle/1471x/2176071
专题高能物理研究所
通讯作者Yang, Yanlian
作者单位1.Chinese Acad Sci, Natl Ctr Nanoscience & Technol, Key Lab Biol Effects Nanomat & Nanosafety, Beijing 100190, Peoples R China
2.Chinese Acad Sci, Natl Ctr Nanoscience & Technol, Key Lab Standardizat & Measurement Nanotechnol, Beijing 100190, Peoples R China
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GB/T 7714
Mao, Xiaobo,Guo, Yuanyuan,Wang, Chenxuan,et al. Binding modes of thioflavin t molecules to prion peptide assemblies identified by using scanning tunneling microscopy[J]. Acs chemical neuroscience,2011,2(6):281-287.
APA Mao, Xiaobo.,Guo, Yuanyuan.,Wang, Chenxuan.,Zhang, Min.,Ma, Xiaojing.,...&Wang, Chen.(2011).Binding modes of thioflavin t molecules to prion peptide assemblies identified by using scanning tunneling microscopy.Acs chemical neuroscience,2(6),281-287.
MLA Mao, Xiaobo,et al."Binding modes of thioflavin t molecules to prion peptide assemblies identified by using scanning tunneling microscopy".Acs chemical neuroscience 2.6(2011):281-287.

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来源:高能物理研究所

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